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Journal ArticleDOI

Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae.

Margaret Werner-Washburne, +2 more
- 01 Jul 1987 - 
- Vol. 7, Iss: 7, pp 2568-2577
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TLDR
Saccharomyces cerevisiae contains a large family of genes related to hsp70, the major heat shock-inducible gene of Drosophila melanogaster, which indicates that SSA3 encodes a functional protein and that the SSA1, SSA2, S SA3, and SSA4 gene products are functionally similar.
Abstract
Saccharomyces cerevisiae contains a large family of genes related to hsp70, the major heat shock-inducible gene of Drosophila melanogaster. One subfamily, identified by sequence homology, contains four genes, SSA1, SSA2, SSA3, and SSA4 (formerly YG100, YG102, YG106, and YG107, respectively). Previous studies showed that strains containing mutations in SSA1 and SSA2 are temperature sensitive for growth. SSA4, which is normally heat inducible and not expressed during vegetative growth, is expressed at high levels in ssa1 ssa2 strains at 23 degrees C. We constructed mutations in SSA3 and SSA4 and analyzed strains carrying mutations in the four genes. Strains carrying mutations in SSA3 SSA4 or SSA3 and SSA4 were indistinguishable from the wild type. However, ssa1 ssa2 ssa4 strains were inviable. SSA3, like SSA4, is a heat-inducible gene that is not normally expressed at 23 degrees C. Nevertheless, an intact copy of SSA3 regulated by the constitutive SSA2 promoter was capable of rescuing a ssa1 ssa2 ssa4 strain. This indicates that SSA3 encodes a functional protein and that the SSA1, SSA2, SSA3, and SSA4 gene products are functionally similar.

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Citations
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The heat-shock proteins

TL;DR: Roles moleculaires des proteines de choc thermique dans le fonctionnement des organismes a des temperatures normales et suite a des chocs thermiques; differents genes impliques.
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Protein folding in the cell.

TL;DR: Folding and assembly of polypeptides in vivo involves other proteins, many of which belong to families that have been highly conserved during evolution.
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The Function of Heat-Shock Proteins in Stress Tolerance: Degradation and Reactivation of Damaged Proteins

TL;DR: The Lon Protease, DnaK.T URNOVER of AB ERR ANT PROT EINS in E. COLI, and more.
Journal ArticleDOI

A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides

TL;DR: Depletion of a subset of 7OK stress proteins in yeast mutants shows that they are involved in the post-translational import of precursor polypeptides into both mitochondria and the lumen of the endoplasmic reticulum.
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The saccharomyces cerevisiae zinc finger proteins msn2p and msn4p are required for transcriptional induction through the stress-response element (stre )

TL;DR: The results suggest that MSN2 and MSN4 encode a DNA‐binding component of the stress responsive system and it is likely that they act as positive transcription factors.
References
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Journal ArticleDOI

Detection of specific sequences among DNA fragments separated by gel electrophoresis.

TL;DR: This paper describes a method of transferring fragments of DNA from agarose gels to cellulose nitrate filters that can be hybridized to radioactive RNA and hybrids detected by radioautography or fluorography.
Journal ArticleDOI

High resolution two-dimensional electrophoresis of proteins.

TL;DR: This technique provides a method for estimation of the number of proteins made by any biological system and can resolve proteins differing in a single charge and consequently can be used in the analysis of in vivo modifications resulting in a change in charge.
Journal ArticleDOI

The heat-shock response

TL;DR: A comparison of different Organisms and Stages of Development and Heat-Induced Lethality and Thermotolerance and the role of RNA Processing are presented.
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